Structure of PDB 6vfs Chain B

Receptor sequence
>6vfsB (length=318) Species: 487 (Neisseria meningitidis) [Search protein sequence]
KLPTPAEIVANLNDHVIGQEQAKKALAVSVYNHYKRLRHKSNILLIGPTG
SGKTLLAQSLARKLDVPFVMADATTLTEAGYVGEDVEQIITKLLGKCDFD
VEKAQRGIVYIDQIDKISRTRDVSGEGVQQALLKLIEGTVASVPPQINVD
TTNILFICGGAFAGLEKVIRQRTEKGGIGFGASVHADITKLFGIVEPEDL
IKFGLIPELIGRLPVIATLEILDEDALINILTEPKNALVKQYQALFGMEN
VELEFEEGALRSIARQAMERKTGARGLRSIVERCLLDTMYRLPDLKGLKK
VVVGKAVIEEGREPELVF
3D structure
PDB6vfs A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
ChainB
Resolution3.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide B G152 Y153 V154 G80 Y81 V82
BS02 ATP B V78 I79 G122 S123 G124 K125 T126 L127 I324 A368 R369 V16 I17 G50 S51 G52 K53 T54 L55 I230 A274 R275
BS03 MG B T126 D184 T54 D112
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
GO:0046983 protein dimerization activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0051301 cell division
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0009376 HslUV protease complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6vfs, PDBe:6vfs, PDBj:6vfs
PDBsum6vfs
PubMed31916936
UniProtQ9JYY3|CLPX_NEIMB ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)

[Back to BioLiP]